1f95

SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

DYNEIN

Rattus norvegicus

UniProt P63170

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 BCL2-LIKE 11 (APOPTOSIS FACILITATOR) × 2 (O43521) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DYL1_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–89; UniProt 1–89 Author chain B; PDBConstruct 1–89; UniProt 1–89

BCL2-LIKE 11 (APOPTOSIS FACILITATOR)

OrganismNot specified

UniProt O43521

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 DYNEIN × 2 (P63170) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name B2L11_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–9; UniProt 108–116 Author chain D; PDBConstruct 1–9; UniProt 108–116

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id1f95
Deposition date deposition_date2000-07-07
Structure title titleSOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX
Keywords keywordsdynein, light chain, DLC8, Bim, APOPTOSIS, CONTRACTILE PROTEIN-peptide complex; CONTRACTILE PROTEIN/peptide
Experimental Method methodSOLUTION NMR
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1f95__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1f95__assembly_1__model_1 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1f95__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)17.48 Å
Rg (electron density)16.20 Å
Total Rg17.54 Å
Atom count3156
Residues196
Excluded volume28299 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1f95__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1f95a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.39 — DLC
Superfamily Superfamily superfamilyd.39.1 — DLC
Family Family familyd.39.1.1 — DLC
Domain ID domain_idd1f95b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.39 — DLC
Superfamily Superfamily superfamilyd.39.1 — DLC
Family Family familyd.39.1.1 — DLC

CATH v4.4 (2 domains)

Domain ID domain_id1f95A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology740 — Protein Inhibitor Of Neuronal Nitric Oxide Synthase
Homologous superfamily homologous superfamily10 — Protein Inhibitor Of Neuronal Nitric Oxide Synthase;
Domain ID domain_id1f95B00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology740 — Protein Inhibitor Of Neuronal Nitric Oxide Synthase
Homologous superfamily homologous superfamily10 — Protein Inhibitor Of Neuronal Nitric Oxide Synthase;
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7. Citations (1)